Lecture 6 - Lecture 6 Protein structure Introduction...

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Lecture 6 Protein structure Introduction Primary structure: amino acid sequence, covalent (peptide) bonds Secondary structure: α -helix, ß-sheets, repeating H-bonds Tertiary structure: side-chain bonds: H-, ionic, hydrophobic, VdW, disulfide (within chain) Quaternary structure: side-chain bonds (between chains) Primary structure amino acid sequence, covalent (peptide) bonds: from previous lecture Secondary structure Primary bond influence: recall that planar amide bond constrains chain’s bends planes: no rotation around CO-N bonds, but planes rotate around α -C-N ( φ ) and α -C- CO bonds ( ψ )
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Ramachandran plot (p. 138) shows grouping of φψ combinations and relates them to common structures in real proteins φ repetitive structures ( α -helix, ß-sheets) are common α -helix (Fig 6.6, p. 140, Fig 6.9, p. 141) 3.6 amino acids per turn 0.54 nm per turn side chains pointed out H-bonds parallel to axis n-4 H-bonds dipole moment (neg. at C end) no pro, less gly, ser limited similar side chain charges
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This note was uploaded on 09/29/2010 for the course VEN 101C 91861 taught by Professor Davidsmart during the Spring '09 term at UC Davis.

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Lecture 6 - Lecture 6 Protein structure Introduction...

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